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  • Title: Characterisation of a carboxypeptidase in human serum distinct from carboxypeptidase N.
    Author: Hendriks D, Scharpé S, van Sande M, Lommaert MP.
    Journal: J Clin Chem Clin Biochem; 1989 May; 27(5):277-85. PubMed ID: 2760564.
    Abstract:
    Arginine carboxypeptidase activity in human serum, measured with the hippuryl-L-arginine substrate, is about three times higher than in human plasma. This difference is much smaller when hippuryl-L-lysine is used as the substrate. When fresh serum is incubated at 30 degrees C, the arginine and lysine carboxypeptidase activity decreases until a stable activity, close to the plasma activity, is reached. This stable carboxypeptidase activity is attributed to carboxypeptidase N. The unstable carboxypeptidase differs from carboxypeptidase N in pH-optimum, esterase activity, substrate specificity, Co2+-activation and dithiotreitol activation. Blood cells are not responsible for the release of this enzyme during coagulation. No activator of carboxypeptidase N was detectable in human serum. Ion-exchange chromatography on DEAE-cellulose confirms the presence of two different molecular forms of arginine carboxypeptidase activity.
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